PMID:20598079
| Citation |
Bennion, D, Charlson, ES, Coon, E and Misra, R (2010) Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli. Mol. Microbiol. 77:1153-71 |
|---|---|
| Abstract |
BamA of Escherichia coli is an essential component of the hetero-oligomeric machinery that mediates β-barrel outer membrane protein (OMP) assembly. The C- and N-termini of BamA fold into trans-membrane β-barrel and five soluble POTRA domains respectively. Detailed characterization of BamA POTRA 1 missense and deletion mutants revealed two competing OMP assembly pathways, one of which is followed by the archetypal trimeric β-barrel OMPs, OmpF and LamB, and is dependent on POTRA 1. Interestingly, our data suggest that BamA also requires its POTRA 1 domain for proper assembly. The second pathway is independent of POTRA 1 and is exemplified by TolC. Site-specific cross-linking analysis revealed that the POTRA 1 domain of BamA interacts with SurA, a periplasmic chaperone required for the assembly of OmpF and LamB, but not that of TolC and BamA. The data suggest that SurA and BamA POTRA 1 domain function in concert to assist folding and assembly of most β-barrel OMPs except for TolC, which folds into a unique soluble α-helical barrel and an OM-anchored β-barrel. The two assembly pathways finally merge at some step beyond POTRA 1 but presumably before membrane insertion, which is thought to be catalysed by the trans-membrane β-barrel domain of BamA. |
| Links |
PubMed PMC2975826 Online version:10.1111/j.1365-2958.2010.07280.x |
| Keywords |
Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Carrier Proteins/metabolism; Cell Membrane/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mutant Proteins/genetics; Mutant Proteins/metabolism; Mutation, Missense; Peptidylprolyl Isomerase/metabolism; Protein Structure, Tertiary; Sequence Deletion |
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